scholarly journals Homozygous deficiency of ubiquitin-ligase ring-finger protein RNF168 mimics the radiosensitivity syndrome of ataxia-telangiectasia

2011 ◽  
Vol 18 (9) ◽  
pp. 1500-1506 ◽  
Author(s):  
S S Devgan ◽  
O Sanal ◽  
C Doil ◽  
K Nakamura ◽  
S A Nahas ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Ataxia Telangiectasia ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Finger Protein

scholarly journals A Bioassay-Guided Fractionation of Rosemary Leaf Extract Identifies Carnosol as a Major Hypertrophy Inducer in Human Skeletal Muscle Cells

Nutrients ◽  
2021 ◽  
Vol 13 (12) ◽  
pp. 4190
Author(s):  
Sylvie Morel ◽  
Gérald Hugon ◽  
Manon Vitou ◽  
Marie Védère ◽  
Françoise Fons ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Muscle Cell ◽  
Ubiquitin Ligase ◽  
Human Skeletal Muscle ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Promoting Effect ◽  
Finger Protein ◽  
Human Skeletal Muscle Cells ◽  
Bioassay Guided Fractionation

A good quality of life requires maintaining adequate skeletal muscle mass and strength, but therapeutic agents are lacking for this. We developed a bioassay-guided fractionation approach to identify molecules with hypertrophy-promoting effect in human skeletal muscle cells. We found that extracts from rosemary leaves induce muscle cell hypertrophy. By bioassay-guided purification we identified the phenolic diterpene carnosol as the compound responsible for the hypertrophy-promoting activity of rosemary leaf extracts. We then evaluated the impact of carnosol on the different signaling pathways involved in the control of muscle cell size. We found that activation of the NRF2 signaling pathway by carnosol is not sufficient to mediate its hypertrophy-promoting effect. Moreover, carnosol inhibits the expression of the ubiquitin ligase E3 Muscle RING Finger protein-1 that plays an important role in muscle remodeling, but has no effect on the protein synthesis pathway controlled by the protein kinase B/mechanistic target of rapamycin pathway. By measuring the chymotrypsin-like activity of the proteasome, we found that proteasome activity was significantly decreased by carnosol and Muscle RING Finger 1 inactivation. These results strongly suggest that carnosol can induce skeletal muscle hypertrophy by repressing the ubiquitin-proteasome system-dependent protein degradation pathway through inhibition of the E3 ubiquitin ligase Muscle RING Finger protein-1.

scholarly journals Ring Finger Protein 149 Is an E3 Ubiquitin Ligase Active on Wild-type v-Raf Murine Sarcoma Viral Oncogene Homolog B1 (BRAF)

2012 ◽  
Vol 287 (28) ◽  
pp. 24017-24025 ◽  
Author(s):  
Seung-Woo Hong ◽  
Dong-Hoon Jin ◽  
Jae-Sik Shin ◽  
Jai-Hee Moon ◽  
Young-Soon Na ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Wild Type ◽  
Viral Oncogene ◽  
Finger Protein ◽  
Type V ◽  
Murine Sarcoma ◽  
Viral Oncogene Homolog

scholarly journals Gid9, a second RING finger protein contributes to the ubiquitin ligase activity of the Gid complex required for catabolite degradation

FEBS Letters ◽  
2011 ◽  
Vol 585 (24) ◽  
pp. 3856-3861 ◽  
Author(s):  
Bernhard Braun ◽  
Thorsten Pfirrmann ◽  
Ruth Menssen ◽  
Kay Hofmann ◽  
Hartmut Scheel ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Finger Protein ◽  
Ubiquitin Ligase Activity

scholarly journals Human RING finger protein ZNF645 is a novel testis-specific E3 ubiquitin ligase

2010 ◽  
Vol 12 (5) ◽  
pp. 658-666 ◽  
Author(s):  
Yun-Qiang Liu ◽  
Gang Bai ◽  
Hao Zhang ◽  
Dan Su ◽  
Da-Chang Tao ◽  
...  
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Finger Protein

Rma1, a novel type of RING finger protein conserved from Arabidopsis to human, is a membrane-bound ubiquitin ligase

2001 ◽  
Vol 114 (10) ◽  
pp. 1949-1957 ◽  
Author(s):  
N. Matsuda ◽  
T. Suzuki ◽  
K. Tanaka ◽  
A. Nakano
Keyword(s):  
Ubiquitin Ligase ◽  
Mutational Analysis ◽  
Ring Finger ◽  
Ring Finger Protein ◽  
Finger Protein ◽  
Ubiquitin Ligase E3 ◽  
Membrane Bound ◽  
E2 Enzymes ◽  
Membrane Anchoring ◽  
Ring Finger Motif

Rma1 is a protein with a RING finger motif and a C-terminal membrane-anchoring domain and is well conserved among higher eukaryotes. We show that fusion proteins between maltose binding protein (MBP) and human or Arabidopsis Rma1 are polyubiquitinated, when incubated with the rabbit reticulocyte or the wheat germ lysate, respectively. The polyubiquitination of MBP-Rma1 has been reconstituted by incubation with purified ubiquitin, the ubiquitin-activating enzyme E1, and one of the two ubiquitin-conjugating E2 enzymes (Ubc4 or UbcH5a). Other E2 enzymes tested, E2-20k, E2-25k, Ubc3 and Ubc8, are not able to confer this modification. Mutational analysis shows that the RING finger motif of Rma1 is necessary for the auto-ubiquitination of MBP-Rma1. Thus, Rma1 represents a novel, membrane-bound type of ubiquitin ligase E3, which probably functions with the Ubc4/5 subfamily of E2. The MBP moiety but not Rma1 itself is ubiquitinated in the auto-ubiquitination reaction of MBP-Rma1. Free MBP in solution is not a substrate of Rma1. These observations indicate that bringing the substrate into its physical vicinity is very important for the action of ubiquitin ligase.

scholarly journals The vertebrate muscle-specific RING finger protein family includes MuRF4 - A novel, conserved E3-ubiquitin ligase

FEBS Letters ◽  
2014 ◽  
Vol 588 (23) ◽  
pp. 4390-4397 ◽  
Author(s):  
Daniel J. Macqueen ◽  
Eduardo N. Fuentes ◽  
Juan Antonio Valdés ◽  
Alfredo Molina ◽  
Samuel A.M. Martin
Keyword(s):  
Ubiquitin Ligase ◽  
E3 Ubiquitin Ligase ◽  
Ring Finger ◽  
Protein Family ◽  
Ring Finger Protein ◽  
Finger Protein ◽  
Vertebrate Muscle
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